Pratap, JV and Ravishankar, R and Vijayan, M (2000) X-ray studies on crystalline complexes involving amino acids and peptides. XXXV. Invariance and variability in amino acid aggregation in the complexes of maleic acid with L-histidine and L-lysine. In: Acta Crystallographica Section B, 56 . pp. 690-696.
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Abstract
The crystal structures of complexes of maleic acid with l-histidine and l-lysine have been determined. The two crystallographically independent amino acid molecules in the l-histidine complex have different closed conformations, while the lysine molecule in its complex has the most favourable conformation sterically with an all-trans sidechain trans to the -carboxylate group. The maleic acid molecules exist as semimaleate ions of similar conformation and contain a symmetric O H O hydrogen bond. Amino acid cations and semimaleate anions aggregate into alternate layers in both the structures. The arrangement of molecules in the histidine layer in l histidine semi- maleate is closer to that in the crystals of the free amino acid than in other l-histidine complexes. On the other hand, the arrangement of lysine molecules in its semi-maleate complex is different from any observed so far. However, the well established characteristic interaction patterns involving amino and carboxylate groups still play a major role in holding the molecules together in the crystal of the complex.
Item Type: | Journal Article |
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Publication: | Acta Crystallographica Section B |
Publisher: | International Union of Crystallography |
Additional Information: | The copyright belongs to International Union of Crystallography |
Keywords: | crystalline complexes;amino acids;peptides;maleic acid;l histidine;l lysine |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 30 Aug 2004 |
Last Modified: | 19 Sep 2010 04:14 |
URI: | http://eprints.iisc.ac.in/id/eprint/1371 |
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